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Crystal structure of arabidopsis ARID5 phd finger in complex with H3K4ME3 peptide

Analyse Crystal structure of arabidopsis ARID5 phd finger in complex with H3K4ME3… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6LQE
Type
protein
Length
63 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
At-rich interactive domain-containing protein 4; 15-mer peptide from histone H3.2
UniProt
Q6NQ79, P59226
Ligands
ZN

Structure

x-ray diffraction · 2 distinct chains · 17% helix, 19% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAt-rich interactive domain-containing protein 4protein5520% helix, 15% strandQ6NQ79
P15-mer peptide from histone H3.2protein80% helix, 50% strandP59226

Ligands and binding sites

  • ZN · Zinc ion · metal · 2 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Interfaces

1 interface between chains.

  • A–P · 510 Ų buried · 13 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (methylation).

Compared structures

  • 6LQE · Crystal structure of Arabidopsis ARID5 PHD finger in complex with H3K4me3 peptide · the same entry in another collection · chain A against A, TM-score 1.00
  • Q6NQ79 · AlphaFold monomer V2.0 prediction for at-rich interactive domain- containing protein 4… · a predicted model of the same protein · chain A against A, TM-score 0.95
  • P59226 · AlphaFold monomer V2.0 prediction for histone H3.2 (P59226) · a predicted model of the same protein · chain P against A, TM-score 0.35

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